The plasma membrane H⁺- ATPase of yeast, encoded by the PMA1 gene, is a predominant membrane protein. Pma1 generates the electrochemical proton gradient that is essential for nutrient uptake by secondary active transport systems. Glucose, the external signal more extensively studied in yeast, triggers post translational modifications that increase the H⁺- ATPase activity. We have demonstrated that this activation is strongly dependent on calcium metabolism and that several proteins are directly involved in the glucose-induced activation of H⁺- ATPase (Trópia, M. J. M. et al. 2006, Biochem. Biophys. Res. Comm. 343: 1234-1243, 2006). Among them Snf3 p, a glucose sensor, seems to work in a parallel way with the protein G Gpa2 p. Moreover, we demonstrated that the role of sensor in this pathway is played by the Snf3 p C-terminal tail.  However, the definition of a model by which this sensor would be operating it was not known. In this work, we show evidences suggesting that Snf3 p could be involved in the control of Pmc1 p activity, a vacuolar calcium pump, that would regulate the calcium availability in the cytosol. We have measured the level of expression of PMC1 gene and the activity of this vacuolar pump in different strains. According our results, Snf3 p seems to be involved in a post-translational regulation of Pmc1 p.